1ne9
From Proteopedia
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Crystal Structure of Weissella viridescens FemX at 1.7 Ang Resolution
Overview
Members of the FemABX protein family are novel therapeutic targets, as, they are involved in the synthesis of the bacterial cell wall. They, catalyze the addition of amino acid(s) on the peptidoglycan precursor, using aminoacylated tRNA as a substrate. We report here the, high-resolution structure of Weissella viridescens L-alanine transferase, FemX and its complex with the UDP-MurNAc-pentapeptide. This is the first, structure example of a FemABX family member that does not possess a, coiled-coil domain. FemX consists of two structurally equivalent domains, separated by a cleft containing the binding site of the, UDP-MurNAc-pentapeptide and a long channel that traverses one of the two, domains. Our structural studies bring new insights into the evolution of, the FemABX and the related GNAT superfamilies, shed light on the, recognition site of the aminoacylated tRNA in Fem proteins, and allowed, manual docking of the acceptor end of the alanyl-tRNAAla.
About this Structure
1NE9 is a Single protein structure of sequence from Weissella viridescens with MG as ligand. Full crystallographic information is available from OCA.
Reference
Crystal structures of Weissella viridescens FemX and its complex with UDP-MurNAc-pentapeptide: insights into FemABX family substrates recognition., Biarrotte-Sorin S, Maillard AP, Delettre J, Sougakoff W, Arthur M, Mayer C, Structure. 2004 Feb;12(2):257-67. PMID:14962386
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